Pyruvate oxidase

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pyruvate oxidase
Identifiers
EC no. 1.2.3.3
CAS no. 9001-96-1
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
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PMC articles
PubMed articles
NCBI proteins

In enzymology, pyruvate oxidase (EC 1.2.3.3) is an enzyme that catalyzes the chemical reaction

+
 
 
O2
H2O2
Pyruvate oxidase
O2
H2O2
 
+ CO2
 

The three substrates of this enzyme are pyruvic acid, phosphate, and oxygen. Its products are acetyl phosphate, carbon dioxide, and hydrogen peroxide. [1] [2] [3]

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is pyruvate:oxygen 2-oxidoreductase (phosphorylating). Other names in common use include pyruvic oxidase, and phosphate-dependent pyruvate oxidase. This enzyme participates in pyruvate metabolism. It has 2 cofactors: FAD, and Thiamin diphosphate.

Structural studies

As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1POW, 1POX, 1V5E, 1V5F, 1V5G, 1Y9D, 2DJI, 2EZ4, 2EZ8, 2EZ9, 2EZT, and 2EZU.

References

  1. Enzyme 1.2.3.3 at KEGG Pathway Database.
  2. Williams FR, Hager LP (1966). "Crystalline flavin pyruvate oxidase from Escherichia coli. I Isolation and properties of the flavoprotein". Arch. Biochem. Biophys. 116 (1): 168–76. doi:10.1016/0003-9861(66)90025-7. PMID   5336022.
  3. Tittmann K, Wille G, Golbik R, Weidner A, Ghisla S, Hubner G (2005). "Radical phosphate transfer mechanism for the thiamin diphosphate- and FAD-dependent pyruvate oxidase from Lactobacillus plantarum Kinetic coupling of intercofactor electron transfer with phosphate transfer to acetyl-thiamin diphosphate via a transient FAD semiquinone/hydroxyethyl-ThDP radical pair". Biochemistry. 44 (40): 13291–303. doi:10.1021/bi051058z. PMID   16201755.